chapter 6shodhganga.inflibnet.ac.in/bitstream/10603/1474/11/11_chapter7.pdf · process biochemistry...

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Chapter 6 224 presence of propyl gallate. These observations strongly indicate the suitability of the enzyme for the production of propyl gallate by transesterification. Based on the results obtained from the present study it is concluded that the marine fungus Aspergillus awamori BTMFW 032 has potential for industrial production of extracellular tannase. Garcinia a natural substrate has scope for use as the ideal source of tannin for maximal tannase production. The characteristics of tannase recognized during the course of this study revealed the extreme acidic nature of the enzyme which has immense scope for exploitation in several applications. Further the stability of the enzyme observed over a wide range of temperature and other characteristics observed with the enzyme adds further evidence to its potentiality for industrial applications. Further studies on tea cream solubilisation and synthesis of propyl gallate testify the potentiality of the enzyme for exploitation in respective industries. The results of the present study strongly indicate ample scope for further research on the biochemistry of the enzyme, structure elucidation and enzyme engineering towards a wide range of applications, besides enriching the knowledge on marine enzymes. Of course there is option for cloning and expressing the gene encoding this tannase enzyme into a domesticated host and expression of the enzyme for industrial production. It may be noted that this is the first report on tannase as well as gallic acid production by a marine fungus. Chapter 7 REFERENCES Abdel-Naby, M.A., Sherif, A.A., El-Tanash, A.B., and Mankarios, A.T. (1999): Immobilization of Aspergillus oryzae tannase and properties of the immobilized enzyme. Journal of Applied Microbiology 87, 108–114. Adachi, O., Watanabe, M., and Yamada, H. (1971): Physicochemical properties of the tannase from Aspergillus flavus. Agricultural Biology and Chemistry 32, 1079-1085. Adachi, O., Watanabe, M., and Yamada, H. (1968): Studies on fungal tannase. Part II. Physicochemical properties of tannase of Aspergillus flavus. Agricultural Biology and Chemistry 32, 1079–1085. Aguilar, C. N., and Gutiérrez-Sánchez, G. (2001): Review: Sources, properties, applications and potential uses of tannin acyl hydrolase. Food Science and Technology 7, 373-382. Aguilar, C. N., Rodriguez, R., Gutierrez-Sanchez, G., Augur, C., Favela-Torres, E., Prado-Barragan, L. A., Ramirez-Coronel, A. and Contreras-Esquivel., J. C. (2007): Microbial tannases: Advances and perspectives. Applied Microbiology and Biotechnology 76, 47-59. Aguilar, C.N. (2000): Induction and Repression of Synthesis of Tannase from Aspergillus niger Aa/20 in Submerged and Solid State Cultures. Mexico: Metropolitan Autonomous University; Ph.D Thesis, (in Spanish). Aguilar, C.N., Augur, C., Favela-Torres, E., and Viniegra-González, G. (2001a): Induction and repression patterns of fungal tannase in solid-state and submerged cultures. Process Biochemistry 36, 565-570. Aguilar, C.N., Augur, C., Favela-Torres, E., and Viniegra-González, G. (2001b): Production of tannase by Aspergillus niger Aa-20 in submerged and solid state fermentation: influence of glucose and tannic acid. Journal of Industrial Microbiology and Biotechnology 26, 296– 302. Aguilar, C.N., Augur, C., Viniegra-González, G., and Favela-Torres, E. (1999): A comparison of methods to determine tannin acyl hydrolase activity. Brazilian Archives of Biology and Technology 42, 355–361. Aguilar, C.N., Favela-Torres, E., Viniegra-González, G., and Augur, C. (2002): Culture conditions dictate protease and tannase production in submerged and solid-state cultures by Aspergillus niger Aa-20. Applied Biochemistry and Biotechnology 102, 407–414.

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Page 1: Chapter 6shodhganga.inflibnet.ac.in/bitstream/10603/1474/11/11_chapter7.pdf · Process Biochemistry 36, 565-570. Aguilar, C.N., Augur, C., Favela-Torres, E., and Viniegra-González,

Chapter 6

224

presence of propyl gallate. These observations strongly indicate the suitability of

the enzyme for the production of propyl gallate by transesterification.

Based on the results obtained from the present study it is concluded that

the marine fungus Aspergillus awamori BTMFW 032 has potential for industrial

production of extracellular tannase. Garcinia a natural substrate has scope for use

as the ideal source of tannin for maximal tannase production. The characteristics of

tannase recognized during the course of this study revealed the extreme acidic

nature of the enzyme which has immense scope for exploitation in several

applications. Further the stability of the enzyme observed over a wide range of

temperature and other characteristics observed with the enzyme adds further

evidence to its potentiality for industrial applications. Further studies on tea cream

solubilisation and synthesis of propyl gallate testify the potentiality of the enzyme

for exploitation in respective industries. The results of the present study strongly

indicate ample scope for further research on the biochemistry of the enzyme,

structure elucidation and enzyme engineering towards a wide range of applications,

besides enriching the knowledge on marine enzymes. Of course there is option for

cloning and expressing the gene encoding this tannase enzyme into a domesticated

host and expression of the enzyme for industrial production. It may be noted that

this is the first report on tannase as well as gallic acid production by a marine

fungus.

Chapter 7

REFERENCES

Abdel-Naby, M.A., Sherif, A.A., El-Tanash, A.B., and Mankarios, A.T. (1999): Immobilization of Aspergillus oryzae tannase and properties of the immobilized enzyme. Journal of Applied Microbiology 87, 108–114.

Adachi, O., Watanabe, M., and Yamada, H. (1971): Physicochemical properties of the tannase from Aspergillus flavus. Agricultural Biology and Chemistry 32, 1079-1085.

Adachi, O., Watanabe, M., and Yamada, H. (1968): Studies on fungal tannase. Part II. Physicochemical properties of tannase of Aspergillus flavus. Agricultural Biology and Chemistry 32, 1079–1085.

Aguilar, C. N., and Gutiérrez-Sánchez, G. (2001): Review: Sources, properties, applications and potential uses of tannin acyl hydrolase. Food Science and Technology 7, 373-382.

Aguilar, C. N., Rodriguez, R., Gutierrez-Sanchez, G., Augur, C., Favela-Torres, E., Prado-Barragan, L. A., Ramirez-Coronel, A. and Contreras-Esquivel., J. C. (2007): Microbial tannases: Advances and perspectives. Applied Microbiology and Biotechnology 76, 47-59.

Aguilar, C.N. (2000): Induction and Repression of Synthesis of Tannase from Aspergillus niger Aa/20 in Submerged and Solid State Cultures. Mexico: Metropolitan Autonomous University; Ph.D Thesis, (in Spanish).

Aguilar, C.N., Augur, C., Favela-Torres, E., and Viniegra-González, G. (2001a): Induction and repression patterns of fungal tannase in solid-state and submerged cultures. Process Biochemistry 36, 565-570.

Aguilar, C.N., Augur, C., Favela-Torres, E., and Viniegra-González, G. (2001b): Production of tannase by Aspergillus niger Aa-20 in submerged and solid state fermentation: influence of glucose and tannic acid. Journal of Industrial Microbiology and Biotechnology 26, 296–302.

Aguilar, C.N., Augur, C., Viniegra-González, G., and Favela-Torres, E. (1999): A comparison of methods to determine tannin acyl hydrolase activity. Brazilian Archives of Biology and Technology 42, 355–361.

Aguilar, C.N., Favela-Torres, E., Viniegra-González, G., and Augur, C. (2002): Culture conditions dictate protease and tannase production in submerged and solid-state cultures by Aspergillus niger Aa-20. Applied Biochemistry and Biotechnology 102, 407–414.

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